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- PDB-2flg: Solution structure of an EGF-LIKE domain from the Plasmodium falc... -

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Basic information

Entry
Database: PDB / ID: 2flg
TitleSolution structure of an EGF-LIKE domain from the Plasmodium falciparum merozoite surface protein 1
ComponentsMerozoite surface protein 1
KeywordsSURFACE ACTIVE PROTEIN / EGF-LIKE DOMAIN / EXTRACELLULAR / MODULAR PROTEIN / SURFACE ANTIGEN / MALARIA VACCINE COMPONENT / SURFACE PROTEIN
Function / homology
Function and homology information


vacuolar membrane / side of membrane / extracellular region / plasma membrane
Similarity search - Function
Merozoite surface 1, C-terminal / Merozoite surface protein, EGF domain 1 / Merozoite surface protein 1 (MSP1) C-terminus / MSP1 EGF domain 1 / Laminin / Laminin / Ribbon / Mainly Beta
Similarity search - Domain/homology
Merozoite surface protein 1
Similarity search - Component
MethodSOLUTION NMR / torsion angle dynamics
AuthorsJames, S. / Moehle, K. / Pluschke, G. / Robinson, J.
CitationJournal: Chembiochem / Year: 2006
Title: Synthesis, solution structure and immune recognition of an epidermal growth factor-like domain from Plasmodium falciparum merozoite surface protein-1.
Authors: James, S. / Moehle, K. / Renard, A. / Mueller, M.S. / Vogel, D. / Zurbriggen, R. / Pluschke, G. / Robinson, J.A.
History
DepositionJan 6, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 21, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Nov 6, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Merozoite surface protein 1


Theoretical massNumber of molelcules
Total (without water)5,6001
Polymers5,6001
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100STRUCTURES WITH THE LEAST RESTRAINT VIOLATIONS AND LOWEST TARGET FUNCTION
RepresentativeModel #1closest to the average

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Components

#1: Protein/peptide Merozoite surface protein 1 / Merozoite surface antigens / PMMSA / P195


Mass: 5600.310 Da / Num. of mol.: 1 / Fragment: C-TERMINAL FRAGMENT, residues 1526-1573 / Source method: obtained synthetically
Details: The protein occurs naturally in Plasmodium falciparum
References: UniProt: P04933
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1212D TOCSY
131DQF-COSY

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Sample preparation

DetailsContents: 1.25 MM FIRST N-TERMINAL EGF-LIKE DOMAIN of MSP1(19), 90% H2O, 10% D2O
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 0 mM / pH: 5 / Pressure: 1 atm / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
XwinNMR2.6processing
XEASY1.53data analysis
CYANA2.1P.GUNTERT ET AL.structure solution
CYANA2.1P.GUNTERT ET AL.refinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: closest to the average
NMR ensembleConformer selection criteria: STRUCTURES WITH THE LEAST RESTRAINT VIOLATIONS AND LOWEST TARGET FUNCTION
Conformers calculated total number: 100 / Conformers submitted total number: 20

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